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1vk1
From Proteopedia
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| - | [[Image:1vk1.jpg|left|200px]]<br /><applet load="1vk1" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1vk1, resolution 1.20Å" /> | ||
| - | '''Conserved hypothetical protein from Pyrococcus furiosus Pfu-392566-001'''<br /> | ||
| - | == | + | ==Conserved hypothetical protein from Pyrococcus furiosus Pfu-392566-001== |
| - | + | <StructureSection load='1vk1' size='340' side='right'caption='[[1vk1]], [[Resolution|resolution]] 1.20Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1vk1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VK1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VK1 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vk1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vk1 OCA], [https://pdbe.org/1vk1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vk1 RCSB], [https://www.ebi.ac.uk/pdbsum/1vk1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vk1 ProSAT], [https://www.topsan.org/Proteins/SECSG/1vk1 TOPSAN]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/Q8U3S5_PYRFU Q8U3S5_PYRFU] | |
| - | + | == Evolutionary Conservation == | |
| - | + | [[Image:Consurf_key_small.gif|200px|right]] | |
| - | [ | + | Check<jmol> |
| - | + | <jmolCheckbox> | |
| - | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vk/1vk1_consurf.spt"</scriptWhenChecked> | |
| - | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |
| - | + | <text>to colour the structure by Evolutionary Conservation</text> | |
| - | + | </jmolCheckbox> | |
| - | [ | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1vk1 ConSurf]. |
| - | [[ | + | <div style="clear:both"></div> |
| - | + | <div style="background-color:#fffaf0;"> | |
| - | + | == Publication Abstract from PubMed == | |
| - | [ | + | BACKGROUND: The major bottleneck for determination of 3 D structures of proteins using X-rays is the production of diffraction quality crystals. Often proteins are subjected to chemical modification to improve the chances of crystallization RESULTS: Here, we report the successful crystallization of a nuclease employing a reductive methylation protocol. The key to crystallization was the successful introduction of 44 new cohesive (NZ) CH...O contacts (3.2-3.7 A) by the addition of 2 methyl groups to the side chain amine nitrogen (NZ) of 9 lysine residues of the nuclease. The new contacts dramatically altered the crystallization properties of the protein, resulting in crystals that diffracted to 1.2 A resolution. Analytical ultracentrifugation analysis and thermodynamics results revealed a more compact protein structure with better solvent exclusion of buried Trp residues in the folded state of the methylated protein, assisting crystallization. CONCLUSION: In this study, introduction of novel cohesive (NZ)CH...O contacts by reductive methylation resulted in the crystallization of a protein that had previously resisted crystallization in spite of extensive purification and crystallization space screening. Introduction of (NZ)CH...O contacts could provide a solution to crystallization problems for a broad range of protein targets. |
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| - | + | (NZ)CH...O contacts assist crystallization of a ParB-like nuclease.,Shaw N, Cheng C, Tempel W, Chang J, Ng J, Wang XY, Perrett S, Rose J, Rao Z, Wang BC, Liu ZJ BMC Struct Biol. 2007 Jul 7;7:46. PMID:17617922<ref>PMID:17617922</ref> | |
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 1vk1" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pyrococcus furiosus]] | ||
| + | [[Category: Adams MWW]] | ||
| + | [[Category: Brereton PS]] | ||
| + | [[Category: Chang J]] | ||
| + | [[Category: Chen L]] | ||
| + | [[Category: Izumi M]] | ||
| + | [[Category: Jenney Jr FE]] | ||
| + | [[Category: Lee D]] | ||
| + | [[Category: Liu ZJ]] | ||
| + | [[Category: Ng J]] | ||
| + | [[Category: Poole II FL]] | ||
| + | [[Category: Richardson DC]] | ||
| + | [[Category: Richardson JS]] | ||
| + | [[Category: Rose J]] | ||
| + | [[Category: Shah A]] | ||
| + | [[Category: Shah C]] | ||
| + | [[Category: Sugar FJ]] | ||
| + | [[Category: Tempel W]] | ||
| + | [[Category: Wang BC]] | ||
| + | [[Category: Yang H]] | ||
| + | [[Category: Zhao M]] | ||
Current revision
Conserved hypothetical protein from Pyrococcus furiosus Pfu-392566-001
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Categories: Large Structures | Pyrococcus furiosus | Adams MWW | Brereton PS | Chang J | Chen L | Izumi M | Jenney Jr FE | Lee D | Liu ZJ | Ng J | Poole II FL | Richardson DC | Richardson JS | Rose J | Shah A | Shah C | Sugar FJ | Tempel W | Wang BC | Yang H | Zhao M

